We are studying the- structure of the yeast ribosomal protein L32. Although the ribosomal RNA binding site of this protein is not known, it autoregulates the expression of its own mRNA by binding to the 5'-splice site and regulating splicing of the pre-mRNA. The binding site of the mRNA has been characterized to be a stem-loop structure. As a prelude to characterization of the RNAprotein complex, we are studying the solution structure of the L32 protein. We have collected > 1500 NOEs for the structure of the free protein. Preliminary structure calculations indicate the protein is a beta sheet motif with alpha helices packed on both sides of the sheet. Refinement of the structure is in progress.